ID A0A0F8UL09_9EURO Unreviewed; 406 AA.
AC A0A0F8UL09;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=NEDD8-activating enzyme E1 catalytic subunit {ECO:0000256|ARBA:ARBA00015203, ECO:0000256|RuleBase:RU368009};
DE EC=6.2.1.64 {ECO:0000256|ARBA:ARBA00023624, ECO:0000256|RuleBase:RU368009};
GN ORFNames=ARAM_005661 {ECO:0000313|EMBL:KKK20279.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK20279.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK20279.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK20279.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of the dimeric E1 enzyme, which activates
CC NEDD8. {ECO:0000256|RuleBase:RU368009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-
CC cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8
CC protein]-yl-L-cysteine.; EC=6.2.1.64;
CC Evidence={ECO:0000256|ARBA:ARBA00024626,
CC ECO:0000256|RuleBase:RU368009};
CC -!- PATHWAY: Protein modification; protein neddylation.
CC {ECO:0000256|ARBA:ARBA00005032, ECO:0000256|RuleBase:RU368009}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA3
CC subfamily. {ECO:0000256|ARBA:ARBA00006310,
CC ECO:0000256|RuleBase:RU368009}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKK20279.1}.
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DR EMBL; JZBS01002075; KKK20279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8UL09; -.
DR STRING; 308745.A0A0F8UL09; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00885; -.
DR Proteomes; UP000034291; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019781; F:NEDD8 activating enzyme activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045116; P:protein neddylation; IEA:UniProtKB-UniRule.
DR CDD; cd01488; Uba3_RUB; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR Gene3D; 3.10.290.20; Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3; 1.
DR InterPro; IPR014929; E2-binding.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR030468; Uba3_N.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953:SF6; NEDD8-ACTIVATING ENZYME E1 CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF08825; E2_bind; 1.
DR Pfam; PF00899; ThiF; 1.
DR SMART; SM01181; E2_bind; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU368009};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU368009};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU368009};
KW Reference proteome {ECO:0000313|Proteomes:UP000034291};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU368009}.
FT DOMAIN 323..406
FT /note="E2 binding"
FT /evidence="ECO:0000259|SMART:SM01181"
SQ SEQUENCE 406 AA; 45556 MW; 59552C8012F83EFC CRC64;
MAVGDPPLRW KYLYKVLSKS GPSCDPDWVP GEETIECLES SKILVIGAGG LGCEILKNLA
LSGFKDIHFL FRHSDIGKPK AEVAAAFVER RVQGVKITPY VGKIQDKDED YYLQFKMIVC
GLDSIEARRW INSTLIGMVD FENPESLKPL IDGGTEGFKG QARVILPTLS SCIECQLDMH
APRPAVPLCT IATIPRQPQH CIEWAHQIAW QEKRKDDSFD SDDMEHIGWV YNNALERAKQ
FNIFGVTFQM TQGVVKNIIP AIASTNAVIA AATTSEALKI ATSCNPYLEN YMMYAGEEGV
YTYTFEAEKK PDCPVCGNLA RKLTVDPNMT LEAFIETLGE RPEAQLKKPS MRTEEKTLYQ
RFPPQLEEQT RPNLKSKLRD LVADGQEIAV SDPAYTIDFR FQLIFS
//